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Proteomic Alterations During Dormant Period of Curcuma Longa Rhizomes Daranee Chokchaichamnankit1, Pantipa Subhasitanont1, N

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Proteomic Alterations During Dormant Period of Curcuma Longa Rhizomes Daranee Chokchaichamnankit1, Pantipa Subhasitanont1, N Journal of Proteomics & Bioinformatics - Open Access JPB/Vol.2/September 2009 Research Article OPEN ACCESS Freely available online doi:10.4172/jpb.1000098 Proteomic Alterations During Dormant Period of Curcuma Longa Rhizomes Daranee Chokchaichamnankit1, Pantipa Subhasitanont1, N. Monique Paricharttanakul1, Polkit Sangvanich2, Jisnuson Svasti1,3,4, Chantragan Srisomsap1,3,* 1Laboratory of Biochemistry, Chulabhorn Research Institute, Bangkok 10210, Thailand 2Research Center for Bioorganic Chemistry, Department of Chemistry, Faculty of Science, Chulalongkorn University, Bangkok 10330, Thailand 3Chulabhorn Graduate Institute, Bangkok 10210, Thailand 4Department of Biochemistry and Center for Protein Structure and Function, Faculty of Science, Mahidol University, Bangkok 10400, Thailand firmed by contemporary scientific research. These include an- Abstract tioxidant, antiarthritic, antimutagenic, antitumor, antithrombotic, antivenom, antibacterial, antifungal, antiviral, nematocidal, Proteins involved during storage of Curcuma longa choleretic, antihepatotoxic and hemagglutinating activities have not been investigated in detail. Proteins and nucleic (Kumar et al., 2006; Sangvanich et al., 2007). acids are considered to be essential for the sprouting period. As numerous applications of proteomic ap- In plant physiology, dormancy is a period of arrested plant proaches have been reported in many areas of biology, growth. It is a strategy exhibited by many plant species to en- biochemistry and biomedicine, we chose to use able their survival in climates unsuitable for growth such as proteomic technology to study the protein expression winter or dry season. Curcumas will start going dormant (rest- of Curcuma longa (Khaminchun) rhizome during dor- ing) in the fall (October), even in warm tropical climates and mancy and sprouting. Microscale solution-phase iso- the rhizomes will grow during summer (Panneerselvam, 1998). The levels of sugars, starch and the activities of enzymes in- electric focusing (Zoom) was employed to enrich the volved in carbohydrate metabolism, respiration, glycolysis, low abundance proteins in the pH range of 5.4-10 and tricarboxylic acid (TCA) cycle and oxidative pentose phosphate improve the separation of those proteins in the acidic pathway (PPP) have been studied during the early period of range from 3-5.4. Samples were drawn at seven-day dormancy and sprouting (Panneerselvam et al., 2007). intervals from harvest until the commencement of sprouting. The proteomic patterns of the storage period At the molecular level, little is known regarding the protein (0, 14, 21, 42, and 70 days) were studied and identified changes during storage of Curcuma longa. Proteins and nucleic by LC/MS/MS in these two pH ranges. High levels of acids are considered to be essential for the sprouting of potato buds (Tuan and Bonner, 1964). As numerous applications of glyceraldehyde-3-phosphate dehydrogenase, a glyco- proteomic approaches have been reported in many areas of bi- lytic enzyme, were present and in glycosylated and phos- ology, biochemistry and biomedicine, we chose to use phorylated forms. Sporamin, the major storage protein proteomics to study the protein expression of Curcuma longa of the tuberous roots of sweet potato, was highly ex- (Khaminchun) rhizome during dormancy and sprouting. pressed in the dormant period and lower expression was Microscale solution-phase isoelectric focusing (Zoom) was em- detected in the sprouting period. Moreover, the enzyme ployed to enrich the low abundant proteins in the pH range for catalyzing the synthesis of catechin, from 5.4-10 and separate the acidic group (3-5.4) of proteins as leucoanthocyanidin reductase, was found for the first well. The two pH ranges of proteins of different periods of dor- time in the Curcuma longa rhizome. These results rep- mancy of Curcuma longa were compared and proteins identi- resent the first proteomic patterns during the storage fied using LC/MS/MS. period of Curcuma longa. For the rhizomes of Curcuma *Corresponding author: Dr. Chantragan Srisomsap, Laboratory of Bio- longa, visible sprouting was observed within 70 days chemistry, Chulabhorn Research Institute, Vibhavadee Rangsit Road, after harvest. Bangkok 10210, Thailand, Tel: (66-2)-5740622 to 33 ext. 3715; Fax: (66-2)-5740625 ext. 3716, E-mail: [email protected] Keywords: Zingiberaceae; Curcuma; Rhizomes; Enrich; Dor- Received July 10, 2009; Accepted September 23, 2009; Published mancy; Sprouting September 25, 2009 Citation: Chokchaichamnankit D, Subhasitanont P, Paricharttanakul NM, Introduction Sangvanich P, Svasti J, et al. (2009) Proteomic Alteration During Dor- mant Period of Curcuma Longa Rhizomes. J Proteomics Bioinform 2: Curcuma is a perennial herb of the family Zingiberaceae. The 380-387. doi:10.4172/jpb.1000098 rhizome of Curcuma, commonly called turmeric (Curcuma Copyright: © 2009 Chokchaichamnankit D, et al. This is an open-ac- longa L.), has been used for centuries as spice and coloring cess article distributed under the terms of the Creative Commons Attri- agent. Turmeric is indigenous to South, Southwest and South- bution License, which permits unrestricted use, distribution, and repro- east Asia. The traditional uses of turmeric in folk medicines are duction in any medium, provided the original author and source are cred- multiple and many of the therapeutic effects have been con- ited. J Proteomics Bioinform Volume 2(9) : 380-387 (2009) - 380 ISSN:0974-276X JPB, an open access journal Journal of Proteomics & Bioinformatics - Open Access JPB/Vol.2/September 2009 Methods Two-dimensional Polyacrylamide Gel electrophoresis (2-D PAGE) Protein Extraction 2-D PAGE was performed using the immobiline/polyacryla- Fresh rhizomes of Curcuma longa were harvested from mide system. Samples were applied by overnight in-gel Ratchaburi province after the aerial parts have fully dried up rehydration of 70 mm ( analytical runs ). pH 4-7 IPG gel strips and stored in the dark. This period is considered to be the initial (GE Healthcare, Biosciences, Uppsala, Sweden) were used for period of dormancy. Mature healthy rhizomes of uniform size samples not enriched by Zoom, whereas non-linear pH 3-10 and weight were kept at 28±2ºC and relative humidity of 65- and 3.9-5.1IPG gel strips were used for samples enriched. The first dimen- 75% in a biophotochamber. Samples were collected at 7-day sion (IEF) was performed at 6,500 Vh, using a Pharmacia LKB intervals from harvest until sprouting. Multiphor II system. The IPG strips were equilibrated in two steps of equilibration buffer. The first step employed 50 mM Curcuma longa rhizomes (15 grams) were peeled to remove Tris-HCl buffer, pH 6.8, 6 M urea, 30% glycerol, 1% SDS and the skin before ground in liquid nitrogen using a mortar and 1% DTT, while 2.5% iodoacetamide replaced DTT in the pestle, and suspended in 30 ml of extraction buffer (0.7 M su- second step. The IPG strips were then applied to the crose, 0.5 M Tris-HCl, 30 mM HCl, 0.1 M KCl and 1% v/v β- second dimension 14% T SDS polyacrylamide gels mercaptoethanol). The mixture was extensively homogenized (100x80x1.5mm). Electrophoresis of the mini-gel was per- and stored at 4°C for at least 30 minutes. After centrifugation at formed in a Hoefer system at 20 mA for two hours at room 4,000g for 10 minutes, the supernatant was transferred and kept temperature. After electrophoresis, proteins were visualized by at 4°C. The plant tissues were resuspended in extraction buffer CBR-250 staining. two times. Fifty milliliters of water-saturated phenol was added to the supernatant, mixed and kept at 4°C for 60 minutes. After Gel Scanning and Image Analysis centrifugation at 8,000g for 10 minutes, the upper phenol phase was removed and resuspended twice in water-saturated phenol Gels were scanned using an ImageScanner II (GE Healthcare, (Hurkman and Tanaka, 1986). Proteins were precipitated from Uppsala, Sweden). The ImageMasterTM (GE Healthcare, the phenol phase of 200 ml 0.1 M ammonium acetate, dissolved Uppsala, Sweden) was used for computer analysis. in methanol and stored overnight at – 20°C. The sample was Tryptic In-gel Digestion centrifuged at 4,000g for 10 minutes. The pellet was dissolved in 10 ml of cold water and sonicated for 3 minutes. The pro- Protein spots were excised and transferred to 0.5 ml microfuge teins were precipitated in 9 volumes of cold acetone. The solu- tubes. Fifty µl of 0.1 M NH4HCO3 in 50% acetonitrile was tion was left at -20 C for at least 4 hours and then centrifuged added. The gel was incubated 3 times for 20 minutes at 30°C. at 4,000g for 10 minutes. The supernatant was discarded and The solvent was discarded and gel particles were dried com- the pellet was air-dried briefly until the smell of acetone had pletely by Speed Vac. Reduction and alkylation was performed disappeared. The amount of protein was determined by using by swelling the gel pieces in 50 µl buffer solution (0.1 M Bradford method. NH4HCO3, 10 mM DTT and 1 mM EDTA) and incubating at 60°C for 45 minutes. After cooling, the excess liquid was re- Microscale Solution-phase Isoelectric Focusing (Zoom) of moved and quickly replaced by the same volume of freshly Protein Extract prepared 100 mM iodoacetamide in 0.1 M NH4HCO3 solution. For in-solution IEF fractionation, a microscale solution-phase The reaction was incubated at room temperature in the dark for isoelectric focusing (ZOOM) IEF fractionator was used 30 minutes. The iodoacetamide solution was removed and the (Invitrogen, Carlsbad, CA, USA). Proteins were reduced by gel pieces were washed with 50% acetonitrile in water, 3 times dissolving with 50 mM DTT (USB Corporation Cleveland, OH, for 10 minutes each time, and the gel pieces were completely USA), 7.7 M urea (ICN), 2.2 M thiourea (Sigma, St Louis, MO, dried. Aliquots of trypsin (Promega Corporation, WI, USA) (1 USA), and 4.4% CHAPS (Calbiochem, San Diego, CA, USA). µg trypsin /10 µl 1% acetic acid) were prepared and stored at The reduced proteins were then alkylated by adding 100 mM -20°C Fifty µl of digestion buffer (0.05 M Tris HCl, 10% ac- iodoacetamide for 30 min and incubated in the dark.
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